Q01594 (ALLN1_ALLSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Alliin lyase 1 Short name=Alliinase-1 EC=4.4.1.4 Alternative name(s): Cysteine sulphoxide lyase 1
Organism	Allium sativum (Garlic)
Taxonomic identifier	4682 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › Asparagales › Amaryllidaceae › Allioideae › Allieae › Allium

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Able to cleave the C-S bond of sulfoxide derivatives of Cys to produce allicin, thus giving rise to all sulfur compounds which are responsible for most of the properties of garlic, such as the specific smell and flavor as well as the health benefits like blood lipid or blood pressure lowering.
Catalytic activity	An S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer. Ref.3
Subcellular location	Vacuole.
Tissue specificity	Bulb and shoots.
Domain	The 6 Cys residues of the EGF-like domain are arranged in a disulfide pattern different from the one found in the canonical EGFs. The function of this domain is unclear. It may be a binding site for other proteins or the docking site for a putative alliinase receptor.
Sequence similarities	Belongs to the alliinase family. Contains 1 EGF-like domain.

Ontologies

Keywords
Cellular component	Vacuole
Domain	EGF-like domain Signal
Ligand	Chloride Pyridoxal phosphate
Molecular function	Lyase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Cellular_component	vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alliin lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Propeptide

29 – 38

10

PRO_0000020677

Chain

39 – 486

448

Alliin lyase 1

PRO_0000020678

Regions

Domain

51 – 97

47

EGF-like; atypical

Sites

Binding site

132

1

Chloride

Binding site

136

1

Chloride

Binding site

138

1

Chloride

Amino acid modifications

Modified residue

289

1

N6-(pyridoxal phosphate)lysine

Glycosylation

57

1

N-linked (GlcNAc...) Potential

Glycosylation

184

1

N-linked (GlcNAc...)

Glycosylation

229

1

N-linked (GlcNAc...) Potential

Glycosylation

366

1

N-linked (GlcNAc...)

Disulfide bond

58 ↔ 77

Disulfide bond

79 ↔ 88

Disulfide bond

82 ↔ 95

Disulfide bond

406 ↔ 414

Secondary structure

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486

Helix Strand Turn

Details...

Helix

44 – 54

11

Helix

59 – 61

3

Beta strand

83 – 85

3

Helix

105 – 107

3

Helix

108 – 111

4

Helix

115 – 118

4

Beta strand

120 – 122

3

Turn

124 – 127

4

Beta strand

129 – 131

3

Helix

141 – 154

14

Beta strand

163 – 168

6

Helix

169 – 181

13

Turn

185 – 187

3

Beta strand

194 – 198

5

Helix

204 – 212

9

Beta strand

218 – 223

6

Helix

224 – 227

4

Helix

233 – 235

3

Beta strand

236 – 243

8

Turn

245 – 247

3

Beta strand

259 – 263

5

Turn

269 – 271

3

Beta strand

281 – 286

6

Helix

287 – 290

4

Helix

294 – 296

3

Beta strand

299 – 303

5

Helix

306 – 319

14

Beta strand

320 – 322

3

Helix

325 – 345

21

Helix

352 – 371

20

Beta strand

374 – 378

5

Beta strand

386 – 388

3

Turn

389 – 392

4

Beta strand

393 – 395

3

Beta strand

400 – 406

7

Helix

409 – 411

3

Helix

414 – 420

7

Helix

428 – 431

4

Beta strand

437 – 441

5

Helix

446 – 460

15

Sequences

	Sequence		Length	Mass (Da)
	Q01594 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: D7862E867AD74383	FASTA	486	55,639
	10 20 30 40 50 60 MVESYKKIGS CNKMPCLVIL TCIIMSNSLV NNNNMVQAKM TWTMKAAEEA EAVANINCSE 70 80 90 100 110 120 HGRAFLDGII SEGSPKCECN TCYTGPDCSE KIQGCSADVA SGDGLFLEEY WKQHKEASAV 130 140 150 160 170 180 LVSPWHRMSY FFNPVSNFIS FELEKTIKEL HEVVGNAAAK DRYIVFGVGV TQLIHGLVIS 190 200 210 220 230 240 LSPNMTATPD APESKVVAHA PFYPVFREQT KYFNKKGYVW AGNAANYVNV SNPEQYIEMV 250 260 270 280 290 300 TSPNNPEGLL RHAVIKGCKS IYDMVYYWPH YTPIKYKADE DILLFTMSKF TGHSGSRFGW 310 320 330 340 350 360 ALIKDESVYN NLLNYMTKNT EGTPRETQLR SLKVLKEVVA MVKTQKGTMR DLNTFGFKKL 370 380 390 400 410 420 RERWVNITAL LDQSDRFSYQ ELPQSEYCNY FRRMRPPSPS YAWVKCEWEE DKDCYQTFQN 430 440 450 460 470 480 GRINTQNGVG FEASSRYVRL SLIKTQDDFD QLMYYLKDMV KAKRKTPLIK QLFIDQTETA SRRPFI

References

[1]	"Isolation and characterization of alliinase cDNA clones from garlic (Allium sativum L.) and related species." van Damme E.J.M., Smeets K., Torrekens S., van Leuven F., Peumans W.J. Eur. J. Biochem. 209:751-757(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-58. Tissue: Shoot.
[2]	"Purification, characterization, and crystallization of alliinase from garlic." Kuettner E.B., Hilgenfeld R., Weiss M.S. Arch. Biochem. Biophys. 402:192-200(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, CRYSTALLIZATION. Tissue: Bulb.
[3]	"The active principle of garlic at atomic resolution." Kuettner E.B., Hilgenfeld R., Weiss M.S. J. Biol. Chem. 277:46402-46407(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 39-465, SUBUNIT. Tissue: Bulb.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

What's that smell? - Issue 39 of October 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z12622 mRNA. Translation: CAA78268.1.

PIR

S29302.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LK9	X-ray	1.53	A/B	39-486	[»]
2HOR	X-ray	1.60	A	39-465	[»]
2HOX	X-ray	1.40	A/B/C/D	39-465	[»]

ProteinModelPortal

Q01594.

SMR

Q01594. Positions 39-465.

ModBase

Search...

Protein family/group databases

Allergome

843. All s Alliin lyase.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13504.

Family and domain databases

Gene3D

2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Pfam

PF04864. Alliinase_C. 1 hit.
PF04863. EGF_alliinase. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00022. EGF_1. 1 hit.
PS01186. EGF_2. False negative.
PS50026. EGF_3. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q01594.

Entry information

Entry name

ALLN1_ALLSA

Accession

Primary (citable) accession number: Q01594

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program